Binding studies of [H]Lyngbyatoxin A and [H]debromoaplysiatoxin to the phorbol ester receptor in a mouse epidermal particulate fraction
- 1 January 1986
- journal article
- research article
- Published by Oxford University Press (OUP) in Carcinogenesis: Integrative Cancer Research
- Vol. 7 (4) , 641-644
- https://doi.org/10.1093/carcin/7.4.641
Abstract
The preparation of [H]lyngbyatoxin A by catalytic triton-proton exchange of lyngbyatoxin A and [H]debromoaplysia-toxin by tritiation - debromination of aplysiatoxin is described. The dose-response curves for the binding of [H]lyng-byatoxin A and [H]debromoaplysiatoxin to a mouse epidermal particulate fraction are virtually the same as the one previously described for [H]12-O-tetradecanoylphorbol-13-acetate ([HTPA). The specific binding of [HTPA, [H]-lyngbyatoxin A and [H]debromoaplysiatoxin to the mouse epidermal particulate fraction is inhibited to the same degree by unlabeled TPA, teleocidin, lyngbyatoxin A, aplysiatoxin and debromoaplysiatoxin. This study indicates that TPA, lyngbyatoxin A and debromoaplysiatoxin bind to the same high affinity receptor in mouse skin.This publication has 6 references indexed in Scilit:
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